Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1974 Sep;141(3):721–723. doi: 10.1042/bj1410721

The interaction of the phosphonate analogue of 3-phospho-d-glycerate with phosphoglycerate kinase

George A Orr 1, Jeremy R Knowles 1
PMCID: PMC1168177  PMID: 4463959

Abstract

The methylene analogue of 3-phospho-d-glycerate, 2-hydroxy-4-phosphono-dl-butyric acid, is a substrate for phosphoglycerate kinase. The pKa values for the final dissociation of the natural substrate and its methylene isostere are 6.20 and 7.45 respectively. The kinetic parameters Km and kcat. for the enzyme-catalysed reaction were determined at pH6.9 and 8.5 by using low substrate concentrations. Although the kcat. values for the two substrates at each pH are similar, there is a 60-fold increase in the Km value for the methylene isostere on going to the lower pH. The results are most readily interpreted in terms of a dianionic group on C-3 being required for efficient substrate binding to the enzyme.

Full text

PDF
721

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams P. R., Harrison R. Dehydration of a phosphonate substrate analogue by glycerol 3-phosphate dehydrogenase. Biochem J. 1974 Sep;141(3):729–732. doi: 10.1042/bj1410729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DOWD J. E., RIGGS D. S. A COMPARISON OF ESTIMATES OF MICHAELIS-MENTEN KINETIC CONSTANTS FROM VARIOUS LINEAR TRANSFORMATIONS. J Biol Chem. 1965 Feb;240:863–869. [PubMed] [Google Scholar]
  3. Dixon H. B., Sparkes M. J. Phosphonomethyl analogues of phosphate ester glycolytic intermediates. Biochem J. 1974 Sep;141(3):715–719. doi: 10.1042/bj1410715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fitzgerald J. W., Thomas P., Tudball N., Winterburn P. J. Preparation of D-glycerate 3-O-sulphate, DL- glycerate 3( 35 S)-O-sulphate and D-glucose 6-O-sulphate. Biochem J. 1971 Feb;121(3):529–530. doi: 10.1042/bj1210529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Krietsch W. K., Bücher T. 3-phosphoglycerate kinase from rabbit sceletal muscle and yeast. Eur J Biochem. 1970 Dec;17(3):568–580. doi: 10.1111/j.1432-1033.1970.tb01202.x. [DOI] [PubMed] [Google Scholar]
  6. Larsson-Raźnikiewicz M. Complex formation between 3-phospho-D-glyceric acid and divalent metal ions. Eur J Biochem. 1972 Nov 7;30(3):579–583. doi: 10.1111/j.1432-1033.1972.tb02129.x. [DOI] [PubMed] [Google Scholar]
  7. Larsson-Raźnikiewicz M. Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion. Biochim Biophys Acta. 1967 Jan 11;132(1):33–40. doi: 10.1016/0005-2744(67)90189-1. [DOI] [PubMed] [Google Scholar]
  8. Morrison J. F., Heyde E. Enzymic phosphoryl group transfer. Annu Rev Biochem. 1972;41(10):29–54. doi: 10.1146/annurev.bi.41.070172.000333. [DOI] [PubMed] [Google Scholar]
  9. Scopes R. K. An improved procedure for the isolation of 3-phosphoglycerate kinase from yeast. Biochem J. 1971 Mar;122(1):89–92. doi: 10.1042/bj1220089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Stribling D. Properties of the phosphonomethyl isosteres of two phosphate ester glycolytic intermediates. Biochem J. 1974 Sep;141(3):725–728. doi: 10.1042/bj1410725. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES